title: Förster resonance energy transfer methods for quantification of protein-protein interactions on microarrays.
abstract: Methods based on Förster (or fluorescence) resonance energy transfer (FRET) are widely used in various areas of bioanalysis and molecular biology, such as fluorescence microscopy, quantitative real-time polymerase chain reaction (PCR), immunoassays, or enzyme activity assays, just to name a few. In the last years, these techniques were successfully implemented to multiplex biomolecular screening on microarrays. In this review, some fundamental considerations and practical approaches are outlined and it is demonstrated how this very sensitive (and distance-dependent) method can be utilized for microarray-based high-throughput screening (HTS) with a focus on protein microarrays. The advantages and also the demands of this dual-label technique in miniaturized multiplexed formats are discussed with respect to its potential readout modes, such as intensity, dual wavelength, and time-resolved FRET detection.
authors.affiliation: Institute of Analytical Chemistry, Chemo- and Biosensors, University of Regensburg, Regensburg, Germany. michael.schaeferling@chemie.uni-regensburg.de
authors.forename: Michael
authors.initials: M
authors.lastname: Schäferling
authors.forename: Stefan
authors.initials: S
authors.lastname: Nagl
mesh_terms: D000818:Animals; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods*; D006801:Humans; D040081:Protein Array Analysis / Q000379:methods*; D025941:Protein Interaction Mapping / Q000379:methods*; D013997:Time Factors